MANC_DICDI
ID MANC_DICDI Reviewed; 1079 AA.
AC Q55ER0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Alpha-mannosidase C;
DE EC=3.2.1.24;
DE Flags: Precursor;
GN Name=manC; ORFNames=DDB_G0268994;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-mannose residues
CC in alpha-D-mannosides.; EC=3.2.1.24;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family. {ECO:0000305}.
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DR EMBL; AAFI02000004; EAL73086.1; -; Genomic_DNA.
DR RefSeq; XP_646960.1; XM_641868.1.
DR AlphaFoldDB; Q55ER0; -.
DR SMR; Q55ER0; -.
DR STRING; 44689.DDB0231613; -.
DR PaxDb; Q55ER0; -.
DR EnsemblProtists; EAL73086; EAL73086; DDB_G0268994.
DR GeneID; 8616650; -.
DR KEGG; ddi:DDB_G0268994; -.
DR dictyBase; DDB_G0268994; manC.
DR eggNOG; KOG1959; Eukaryota.
DR HOGENOM; CLU_268576_0_0_1; -.
DR InParanoid; Q55ER0; -.
DR OMA; SEAACGY; -.
DR PhylomeDB; Q55ER0; -.
DR Reactome; R-DDI-8853383; Lysosomal oligosaccharide catabolism.
DR PRO; PR:Q55ER0; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0004559; F:alpha-mannosidase activity; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR Gene3D; 1.20.1270.50; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.20.110.10; -; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR015341; Glyco_hydro_38_cen.
DR InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR InterPro; IPR000602; Glyco_hydro_38_N.
DR InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR InterPro; IPR013780; Glyco_hydro_b.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF01074; Glyco_hydro_38N; 1.
DR SMART; SM00872; Alpha-mann_mid; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR SUPFAM; SSF88688; SSF88688; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Glycosidase; Hydrolase; Metal-binding; Reference proteome;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1079
FT /note="Alpha-mannosidase C"
FT /id="PRO_0000327842"
FT ACT_SITE 158
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 475
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 589
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 760
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 769
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 848
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 872
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 912
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1040
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1057
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1079 AA; 124433 MW; AFD4C59A88DDC0C4 CRC64;
MFYKTFGFLF IYLIILISGT LSQKEIDSSN EQPVIEVFLV PHSHCDVGWL KTVEQYYTEN
VTLILNNVIE TLTKDKSKKF NWAEIIYFER WWNDQNETLQ NQVKQLISNK QFYFVGGGWT
QNDEAITDYQ AVINQMTLGH QFLFNQFGIK PEIGWQIDPF GPSTLTPTLF KLMGFKYHVI
NRIDERIKYI FNATEMNIPE SGIMTIEREF EFLWYPSSNN PNISIFTHVL DHHYESPSLT
IVDYEIPNLT YTSGFDFEGN PKINPPITIL NLRFRADLLV KIIKERIDLF RHNNLLLPFG
GDFRFQDSKI EFNNMDKLIK FINSNQKTYG VNIKYSTVDE YFEKVIQDTN INWKEDTTTT
TTTTIPIGGD EFPKLSNLDY FDYTKCDYND YQKYKTCSLY YSGFFSSYSE LKQISRQSDS
LLRIGEFLYS FANLISNNNN NDDDDDDDND FNIQLKEISN ILVQHRNVSG ILTHHDAITG
TAKTKVRDDY LLMLNQVQSN TMNNVIPNIV GYLLSNKSIQ NFDYSCNNTI IMNSPQIGDI
FSISFTNSLG WDRSEYIQIQ LPPSTIVTVY NYNLISIQSQ IVQRFDKDNQ TFLYFNVETP
SLGISTYFII ITSTNDDNVD DDVDKVFGDD ELLIYLLKNG ILSKPILSEI SEISELSSSS
SSSSSSSSSQ ITIGNSKFNL NFNYLNENYN LLTLTSFDDL IENEYSIPIT QNYIEYISGN
DNSYIFKPSG LPVNLKPESP KFYKVTGSLV QMITILYTNN CSQTYIVYNS TTTTTTTTTT
TTTTNNDDSP PLELINDEQY FEIDNIVAAG WNKEIGSQFS SESINNDKTF YTSNGLELIE
RNYKSLFNDT TEFNMIAGNY YPVINTIQIL DNKSKKQLTI LTKQSFGASS QNNGELNLLF
IRRSTDQFVT LNETMNDISN PLIKIKVLFG NSNSIENIRT PHSLLLENPL LPIYSIVSDI
TIDKWISIYN TVFKPFKTSL PYNLHLLTFT KQQQQQQQDF NEDNPLDYFI RFLNIYEISQ
SESFSQPIEF KLTNYFNNFN ITNIRESSLT FNSIINNNTN SIILNPLNLI SLIITISKN
